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Search results 1 to 2 out of 2 for Dock2

Category restricted to ProteinDomain (x)

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Categories

Category: ProteinDomain
Type Details Score
Protein Domain
Type: Family
Description: DOCK family members are evolutionarily conserved guanine nucleotide exchange factors (GEFs) for Rho-family GTPases []. DOCK proteins are required during several cellular processes, such as cell motility and phagocytosis. The N-terminal SH3 domain of the DOCK proteins functions as an inhibitor of GEF, which can be relieved upon its binding to the ELMO1-3 adaptor proteins, after their binding to active RhoG at the plasma membrane [, ]. DOCK family proteins are categorised into four subfamilies based on their sequence homology: DOCK-A subfamily (DOCK1/180, 2, 5), DOCK-B subfamily (DOCK3, 4), DOCK-C subfamily (DOCK6, 7, 8), DOCK-D subfamily (DOCK9, 10, 11) []. This entry represents DOCK2 (dedicator of cytokinesis 2). DOCK2 is involved in cytoskeletal rearrangements required for lymphocyte migration in response of chemokines. It activates RAC1 and RAC2, but not CDC42, by functioning as a guanine nucleotide exchange factor (GEF), which exchanges bound GDP for free GTP. It may also participate in IL2 transcriptional activation via the activation of RAC2 [].
Protein Domain
Type: Family
Description: This entry represents engulfment and cell motility protein 1 (ELMO1) from vertebrates. ELMO1 is a scaffolding component of the Elmo-Dock complex. It interacts with DOCK180, which is essential for activation of Rac GTPase-dependent biological processes. Its C-terminal pleckstrin homology (PH) domain mediates direct interaction to DOCK180 and is critical in Rac signalling []. ELMO1 also interacts with DOCK2 and plays a role in controlling DOCK2 levels and DOCK2-dependent T cell migration in primary lymphocytes [, ]. ELMO1 has been linked to invasive phenotype of cancer cells [, , ].ELMO 1-3 are orthologues of the Caenorhabditis elegans ced-12, which is required for the engulfment of dying cells and cell migration []. They are cytoplasmic adaptor proteins that interact with DOCK family guanine nucleotide exchange factors (GEFs) to promote activation of the small GTPase Rac []. ELMO proteins interact with the SH3-domain of DOCKs via an SH3-binding site to enhance the GEF activity of DOCKs. Regulatory GTPases in the Ras superfamily employ a cycle of alternating GTP binding and hydrolysis, controlled by GEFs and GTPase-activating proteins (GAPs), as essential features of their actions in cells [, ].